A thermostable chitosanase was purified from Bacillus sp. KFB-C108, by fractionation of 30 to 70% saturation with ammonium sulfate, DEAE-Toyopearl chromatography, Butyl-Toyopearl chromatography, and TSK-Gel HW-55F gel filtration. The purified enzyme showed a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the molecular weight was estimated to be 48 kDa. The enzyme degraded soluble chitosan and colloidal chitosan, but did not degrade glycol chitosan, chitin, and the other compounds investigated. There was no effect on the chitosanase activity by treatment with chelating agents, alkylating agents, and various metals investigated, and only cobalt ions inhibited the activity. Optimum temperature and pH were 55°C and 6.5, respectively. The enzyme was stable after heat treatment at 80°C for 10 min or 70°C for 30 min and fairly stable in several organic solvents as well. Chitosan was hydrolyzed to (GlcN)4 as a major product by incubation with the enzyme.
|Number of pages||6|
|Journal||Journal of Microbiology and Biotechnology|
|Publication status||Published - 1998 Jan 1|
- Thermostable enzyme
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology